Rapid and Simple Purification of Lysozyme from the Egg Shell Membrane

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  • KOZUKA Miyuki
    Graduate School of Pharmaceutical Sciences, Hokkaido University
  • MURAO Sato
    Graduate School of Pharmaceutical Sciences, Hokkaido University
  • YAMANE Takuya
    Graduate School of Pharmaceutical Sciences, Hokkaido University
  • INOUE Tsutomu
    Division of Bioscience, Hokkaido System Science Co. Ltd.
  • OHKUBO Iwao
    Department of Nutrition, School of Nursing and Nutrition, Tenshi College
  • ARIGA Hiroyoshi
    Graduate School of Pharmaceutical Sciences, Hokkaido University

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Lysozyme (EC 3.2.1.17) is a hydrolytic enzyme that cleaves the β-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, a major bacterial cell wall polymer. In the food industry, lysozyme is used as an additive mainly in the production of wine and beer. Lysozyme was found to be localized in the egg shell membrane. In this study, we found that lysozyme was easily purified from the egg shell membrane and that the enzyme also had antibacterial activity. Furthermore, we found that the antibacterial activity of purified lysozyme from the egg shell membrane was lower than that of purified lysozyme from the egg white at alkaline pH. The method for rapid purification of lysozyme developed in this study should contribute to the food industry.

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